Candidate Cell and Matrix Interaction Domains on the Collagen Fibril, the Predominant Protein of Vertebrates
Open Access
- 1 July 2008
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 283 (30) , 21187-21197
- https://doi.org/10.1074/jbc.m709319200
Abstract
No abstract availableKeywords
This publication has 69 references indexed in Scilit:
- Collagen fibril architecture, domain organization, and triple-helical conformation govern its proteolysisProceedings of the National Academy of Sciences, 2008
- Y-position cysteine substitution in type I collagen (α1(I) R888C/p.R1066C) is associated with osteogenesis imperfecta/Ehlers-Danlos syndrome phenotypeHuman Mutation, 2007
- A single high-affinity binding site for von Willebrand factor in collagen III, identified using synthetic triple-helical peptidesBlood, 2006
- Microfibrillar structure of type I collagen in situProceedings of the National Academy of Sciences, 2006
- Endo180 Binds to the C-terminal Region of Type I CollagenPublished by Elsevier ,2005
- Covalent Cross-linking of the NC1 Domain of Collagen Type IX to Collagen Type II in CartilageJournal of Biological Chemistry, 2004
- α11β1 Integrin Recognizes the GFOGER Sequence in Interstitial CollagensJournal of Biological Chemistry, 2003
- Hydrolysis of Triple-helical Collagen Peptide Models by Matrix MetalloproteinasesPublished by Elsevier ,2000
- COLLAGENS: Molecular Biology, Diseases, and Potentials for TherapyAnnual Review of Biochemistry, 1995
- Heritable Diseases of CollagenNew England Journal of Medicine, 1984